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Volumn 15, Issue 3, 2011, Pages 421-426

Novel proteins: From fold to function

Author keywords

[No Author keywords available]

Indexed keywords

DUO FERRI PROTEIN; FOUR HELIX BUNDLE PROTEIN; HELIX LOOP HELIX PROTEIN; QUINONE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 79957970893     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2011.03.006     Document Type: Review
Times cited : (52)

References (51)
  • 1
    • 0023812695 scopus 로고
    • Characterization of a helical protein designed from 1st principles
    • Regan L., Degrado W.F. Characterization of a helical protein designed from 1st principles. Science 1988, 241:976-978.
    • (1988) Science , vol.241 , pp. 976-978
    • Regan, L.1    Degrado, W.F.2
  • 2
    • 0025040232 scopus 로고
    • De novo design, expression, and characterization of felix-a 4-helix bundle protein of native-like sequence
    • Hecht M.H., Richardson J.S., Richardson D.C., Ogden R.C. De novo design, expression, and characterization of felix-a 4-helix bundle protein of native-like sequence. Science 1990, 249:884-891.
    • (1990) Science , vol.249 , pp. 884-891
    • Hecht, M.H.1    Richardson, J.S.2    Richardson, D.C.3    Ogden, R.C.4
  • 3
    • 0035471133 scopus 로고    scopus 로고
    • De novo design of proteins-what are the rules?
    • Baltzer L., Nilsson H., Nilsson J. De novo design of proteins-what are the rules?. Chem Rev 2001, 101:3153-3163.
    • (2001) Chem Rev , vol.101 , pp. 3153-3163
    • Baltzer, L.1    Nilsson, H.2    Nilsson, J.3
  • 6
    • 27744547316 scopus 로고    scopus 로고
    • Molecular recognition with designed peptides and proteins
    • Cooper W.J., Waters M.L. Molecular recognition with designed peptides and proteins. Curr Opin Chem Biol 2005, 9:627-631.
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 627-631
    • Cooper, W.J.1    Waters, M.L.2
  • 7
    • 77954265366 scopus 로고    scopus 로고
    • Protein core packing by dynamic combinatorial chemistry
    • Roy L., Case M.A. Protein core packing by dynamic combinatorial chemistry. J Am Chem Soc 2010, 132:8894-8896.
    • (2010) J Am Chem Soc , vol.132 , pp. 8894-8896
    • Roy, L.1    Case, M.A.2
  • 8
    • 16244388916 scopus 로고    scopus 로고
    • Probing metal-protein interactions using a de novo design approach
    • Ghosh D., Pecoraro V.L. Probing metal-protein interactions using a de novo design approach. Curr Opin Chem Biol 2005, 9:97-103.
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 97-103
    • Ghosh, D.1    Pecoraro, V.L.2
  • 9
    • 77949860707 scopus 로고    scopus 로고
    • Designing artificial enzymes by intuition and computation
    • Nanda V., Koder R.L. Designing artificial enzymes by intuition and computation. Nat Chem 2010, 2:15-24.
    • (2010) Nat Chem , vol.2 , pp. 15-24
    • Nanda, V.1    Koder, R.L.2
  • 10
    • 0025644594 scopus 로고
    • A tetrahedral zinc(Ii)-binding site introduced into a designed protein
    • Regan L., Clarke N.D. A tetrahedral zinc(Ii)-binding site introduced into a designed protein. Biochemistry 1990, 29:10878-10883.
    • (1990) Biochemistry , vol.29 , pp. 10878-10883
    • Regan, L.1    Clarke, N.D.2
  • 12
    • 0034612192 scopus 로고    scopus 로고
    • Retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins
    • Lombardi A., Summa C.M., Geremia S., Randaccio L., Pavone V., DeGrado W.F. Retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins. Proc Natl Acad Sci U S A 2000, 97:6298-6305.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6298-6305
    • Lombardi, A.1    Summa, C.M.2    Geremia, S.3    Randaccio, L.4    Pavone, V.5    DeGrado, W.F.6
  • 14
    • 0035059933 scopus 로고    scopus 로고
    • Proton and metal ion-dependent assembly of a model diiron protein
    • Pasternak A., Kaplan S., Lear J.D., DeGrado W.F. Proton and metal ion-dependent assembly of a model diiron protein. Protein Sci 2001, 10:958-969.
    • (2001) Protein Sci , vol.10 , pp. 958-969
    • Pasternak, A.1    Kaplan, S.2    Lear, J.D.3    DeGrado, W.F.4
  • 15
    • 47749146974 scopus 로고    scopus 로고
    • Oxygen reactivity of the biferrous site in the de novo designed four helix bundle peptide DFsc: nature of the 'intermediate' and reaction mechanism
    • Calhoun J.R., Iii C.B., Smith T.J., Thamann T.J., DeGrado W.F., Solomon E.I. Oxygen reactivity of the biferrous site in the de novo designed four helix bundle peptide DFsc: nature of the 'intermediate' and reaction mechanism. J Am Chem Soc 2008, 130:9188-9189.
    • (2008) J Am Chem Soc , vol.130 , pp. 9188-9189
    • Calhoun, J.R.1    Iii, C.B.2    Smith, T.J.3    Thamann, T.J.4    DeGrado, W.F.5    Solomon, E.I.6
  • 17
    • 0037055019 scopus 로고    scopus 로고
    • Comparison of the binding of cadmium(II), mercury(II), and arsenic(III) to the de novo designed peptides TRI L12C and TRI L16C
    • Matzapetakis M., Farrer B.T., Weng T.C., Hemmingsen L., Penner-Hahn J.E., Pecoraro V.L. Comparison of the binding of cadmium(II), mercury(II), and arsenic(III) to the de novo designed peptides TRI L12C and TRI L16C. J Am Chem Soc 2002, 124:8042-8054.
    • (2002) J Am Chem Soc , vol.124 , pp. 8042-8054
    • Matzapetakis, M.1    Farrer, B.T.2    Weng, T.C.3    Hemmingsen, L.4    Penner-Hahn, J.E.5    Pecoraro, V.L.6
  • 18
    • 75649133240 scopus 로고    scopus 로고
    • De novo design of a non-natural fold for an iron-sulfur protein: alpha-helical coiled-coil with a four-iron four-sulfur cluster binding site in its central core
    • Grzyb J., Xu F., Weiner L., Reijerse E.J., Lubitz W., Nanda V., Noy D. De novo design of a non-natural fold for an iron-sulfur protein: alpha-helical coiled-coil with a four-iron four-sulfur cluster binding site in its central core. Biochim Biophys Acta-Bioenerg 2010, 1797:406-413.
    • (2010) Biochim Biophys Acta-Bioenerg , vol.1797 , pp. 406-413
    • Grzyb, J.1    Xu, F.2    Weiner, L.3    Reijerse, E.J.4    Lubitz, W.5    Nanda, V.6    Noy, D.7
  • 19
    • 0141620306 scopus 로고    scopus 로고
    • Mimicking photosynthesis in a computationally designed synthetic metalloprotein
    • Cristian L., Piotrowiak P., Farid R.S. Mimicking photosynthesis in a computationally designed synthetic metalloprotein. J Am Chem Soc 2003, 125:11814-11815.
    • (2003) J Am Chem Soc , vol.125 , pp. 11814-11815
    • Cristian, L.1    Piotrowiak, P.2    Farid, R.S.3
  • 20
    • 0037417760 scopus 로고    scopus 로고
    • Binding of Zn-chlorin to a synthetic four-helix bundle peptide through histidine ligation
    • Razeghifard A.R., Wydrzynski T. Binding of Zn-chlorin to a synthetic four-helix bundle peptide through histidine ligation. Biochemistry 2003, 42:1024-1030.
    • (2003) Biochemistry , vol.42 , pp. 1024-1030
    • Razeghifard, A.R.1    Wydrzynski, T.2
  • 22
    • 1842631425 scopus 로고    scopus 로고
    • The HP-1 maquette: from an apoprotein structure to a structured hemoprotein designed to promote redox-coupled proton exchange
    • Huang S.S., Koder R.L., Lewis M., Wand A.J., Dutton P.L. The HP-1 maquette: from an apoprotein structure to a structured hemoprotein designed to promote redox-coupled proton exchange. Proc Natl Acad Sci U S A 2004, 101:5536-5541.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 5536-5541
    • Huang, S.S.1    Koder, R.L.2    Lewis, M.3    Wand, A.J.4    Dutton, P.L.5
  • 23
    • 24944574297 scopus 로고    scopus 로고
    • Design of amphiphilic protein maquettes: controlling assembly, membrane insertion, and cofactor interactions
    • Discher B.M., Noy D., Strzalka J., Ye S.X., Moser C.C., Lear J.D., Blasie J.K., Dutton P.L. Design of amphiphilic protein maquettes: controlling assembly, membrane insertion, and cofactor interactions. Biochemistry 2005, 44:12329-12343.
    • (2005) Biochemistry , vol.44 , pp. 12329-12343
    • Discher, B.M.1    Noy, D.2    Strzalka, J.3    Ye, S.X.4    Moser, C.C.5    Lear, J.D.6    Blasie, J.K.7    Dutton, P.L.8
  • 24
    • 34447636614 scopus 로고    scopus 로고
    • Detection of heme oxygenase activity in a library of four-helix bundle proteins: towards the de novo synthesis of functional heme proteins
    • Monien B.H., Drepper F., Sommerhalter M., Lubitz W., Haehnel W. Detection of heme oxygenase activity in a library of four-helix bundle proteins: towards the de novo synthesis of functional heme proteins. J Mol Biol 2007, 371:739-753.
    • (2007) J Mol Biol , vol.371 , pp. 739-753
    • Monien, B.H.1    Drepper, F.2    Sommerhalter, M.3    Lubitz, W.4    Haehnel, W.5
  • 26
    • 34247489746 scopus 로고    scopus 로고
    • Redox characteristics of a de novo quinone protein
    • Hay S., Westerlund K., Tommos C. Redox characteristics of a de novo quinone protein. J Phys Chem B 2007, 111:3488-3495.
    • (2007) J Phys Chem B , vol.111 , pp. 3488-3495
    • Hay, S.1    Westerlund, K.2    Tommos, C.3
  • 31
    • 27844496157 scopus 로고    scopus 로고
    • An active enzyme constructed from a 9-amino acid alphabet
    • Walter K.U., Vamvaca K., Hilvert D. An active enzyme constructed from a 9-amino acid alphabet. J Biol Chem 2005, 280:37742-37746.
    • (2005) J Biol Chem , vol.280 , pp. 37742-37746
    • Walter, K.U.1    Vamvaca, K.2    Hilvert, D.3
  • 32
    • 33744927392 scopus 로고    scopus 로고
    • A designed glycoprotein analogue of Gc-MAF exhibits native-like phagocytic activity
    • Bogani F., McConnell E., Joshi L., Chang Y., Ghirlanda G. A designed glycoprotein analogue of Gc-MAF exhibits native-like phagocytic activity. J Am Chem Soc 2006, 128:7142-7143.
    • (2006) J Am Chem Soc , vol.128 , pp. 7142-7143
    • Bogani, F.1    McConnell, E.2    Joshi, L.3    Chang, Y.4    Ghirlanda, G.5
  • 33
    • 41449104758 scopus 로고    scopus 로고
    • Modulation of protein stability by O-glycosylation in a designed Gc-MAF analog
    • Spiriti J., Bogani F., van der Vaart A., Ghirlanda G. Modulation of protein stability by O-glycosylation in a designed Gc-MAF analog. Biophys Chem 2008, 134:157-167.
    • (2008) Biophys Chem , vol.134 , pp. 157-167
    • Spiriti, J.1    Bogani, F.2    van der Vaart, A.3    Ghirlanda, G.4
  • 35
    • 77950828675 scopus 로고    scopus 로고
    • De novo designed coiled-coil proteins with variable conformations as components of molecular electronic devices
    • Shlizerman C., Atanassov A., Berkovich I., Ashkenasy G., Ashkenasy N. De novo designed coiled-coil proteins with variable conformations as components of molecular electronic devices. J Am Chem Soc 2010, 132:5070-5076.
    • (2010) J Am Chem Soc , vol.132 , pp. 5070-5076
    • Shlizerman, C.1    Atanassov, A.2    Berkovich, I.3    Ashkenasy, G.4    Ashkenasy, N.5
  • 37
    • 0001348193 scopus 로고
    • Physical organic-chemistry of benzisoxazoles. 1. Mechanism of base-catalyzed decomposition of benzisoxazoles
    • Casey M.L., Kemp D.S., Paul K.G., Cox D.D. Physical organic-chemistry of benzisoxazoles. 1. Mechanism of base-catalyzed decomposition of benzisoxazoles. J Org Chem 1973, 38:2294-2301.
    • (1973) J Org Chem , vol.38 , pp. 2294-2301
    • Casey, M.L.1    Kemp, D.S.2    Paul, K.G.3    Cox, D.D.4
  • 39
    • 0035810165 scopus 로고    scopus 로고
    • Functional proteins from a random-sequence library
    • Keefe A.D., Szostak J.W. Functional proteins from a random-sequence library. Nature 2001, 410:715-718.
    • (2001) Nature , vol.410 , pp. 715-718
    • Keefe, A.D.1    Szostak, J.W.2
  • 41
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino-acids
    • Kamtekar S., Schiffer J.M., Xiong H.Y., Babik J.M., Hecht M.H. Protein design by binary patterning of polar and nonpolar amino-acids. Science 1993, 262:1680-1685.
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamtekar, S.1    Schiffer, J.M.2    Xiong, H.Y.3    Babik, J.M.4    Hecht, M.H.5
  • 44
    • 35348820567 scopus 로고    scopus 로고
    • Peroxidase activity of de novo heme proteins immobilized on electrodes
    • Das A., Hecht M.H. Peroxidase activity of de novo heme proteins immobilized on electrodes. J Inorg Biochem 2007, 101:1820-1826.
    • (2007) J Inorg Biochem , vol.101 , pp. 1820-1826
    • Das, A.1    Hecht, M.H.2
  • 45
    • 67650022871 scopus 로고    scopus 로고
    • Cofactor binding and enzymatic activity in an unevolved superfamily of de novo designed 4-helix bundle proteins
    • Patel S.C., Bradley L.H., Jinadasa S.P., Hecht M.H. Cofactor binding and enzymatic activity in an unevolved superfamily of de novo designed 4-helix bundle proteins. Protein Sci 2009, 18:1388-1400.
    • (2009) Protein Sci , vol.18 , pp. 1388-1400
    • Patel, S.C.1    Bradley, L.H.2    Jinadasa, S.P.3    Hecht, M.H.4
  • 46
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen R.A. Enzyme recruitment in evolution of new function. Ann Rev Microbiol 1976, 30:409-425.
    • (1976) Ann Rev Microbiol , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 47
    • 32844460390 scopus 로고    scopus 로고
    • Directed evolution of ATP binding proteins from a zinc finger domain by using mRNA display
    • Cho G.S., Szostak J.W. Directed evolution of ATP binding proteins from a zinc finger domain by using mRNA display. Chem Biol 2006, 13:139-147.
    • (2006) Chem Biol , vol.13 , pp. 139-147
    • Cho, G.S.1    Szostak, J.W.2
  • 48
    • 34547958191 scopus 로고    scopus 로고
    • Selection and evolution of enzymes from a partially randomized non-catalytic scaffold
    • 828-U813
    • Seelig B., Szostak J.W. Selection and evolution of enzymes from a partially randomized non-catalytic scaffold. Nature 2007, 448. 828-U813.
    • (2007) Nature , vol.448
    • Seelig, B.1    Szostak, J.W.2
  • 49
    • 79251539227 scopus 로고    scopus 로고
    • De Novo designed proteins from a library of artificial sequences function in Escherichia coli and enable cell growth
    • Fisher M.A., McKinley K.L., Bradley L.H., Viola S.R., Hecht M.H. De Novo designed proteins from a library of artificial sequences function in Escherichia coli and enable cell growth. PLoS ONE 2010, 6:e15364.
    • (2010) PLoS ONE , vol.6
    • Fisher, M.A.1    McKinley, K.L.2    Bradley, L.H.3    Viola, S.R.4    Hecht, M.H.5
  • 50
    • 79957979741 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System, Version 0.99rc6, Schrödinger, LLC
    • The PyMOL Molecular Graphics System, Version 0.99rc6, Schrödinger, LLC.
  • 51
    • 0344392714 scopus 로고    scopus 로고
    • Solution structure of a de novo protein from a designed combinatorial library
    • Wei Y.N., Kim S., Fela D., Baum J., Hecht M.H. Solution structure of a de novo protein from a designed combinatorial library. Proc Natl Acad Sci U S A 2003, 100:13270-13273.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 13270-13273
    • Wei, Y.N.1    Kim, S.2    Fela, D.3    Baum, J.4    Hecht, M.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.